Glycine-replaced epinecidin-1 variant bestows better stability and stronger antimicrobial activity against a range of nosocomial pathogenic bacteria.
antimicrobial peptide
epinecidin‐1
multidrug resistance
thioredoxin fusion
Journal
Biotechnology and applied biochemistry
ISSN: 1470-8744
Titre abrégé: Biotechnol Appl Biochem
Pays: United States
ID NLM: 8609465
Informations de publication
Date de publication:
21 Jul 2024
21 Jul 2024
Historique:
received:
31
12
2023
accepted:
29
06
2024
medline:
22
7
2024
pubmed:
22
7
2024
entrez:
22
7
2024
Statut:
aheadofprint
Résumé
Epinecidin-1 (epi-1), an antimicrobial peptide first identified in marine grouper fish, has multifunctional bioactivities. The present study aims to improve its therapeutic potential via structural modifications that could enhance its antimicrobial activity and stability. To achieve it, we replaced glycine and the first histidine in the parent epi-1 with lysine, which resulted in a peptide with a repeating KXXK motif and improved physiochemical properties related to antimicrobial activity. This modified peptide, referred to as glycine-to-lysine replaced-epi-1, also gained stability and a twofold increase in helical propensity. To produce the active peptide, overlap extension PCR was employed to generate the gene of GK-epi-1 via site-directed mutagenesis, which was then cloned into the pET-32a vector and expressed as a recombinant fusion protein in Escherichia coli C43 (DE3) strain. The recombinant protein was purified and digested with enterokinase to release the active peptide fragment, which was then evaluated for antimicrobial activity and stability. The lysine substitution led to an enhancement in broad-spectrum antimicrobial activity against a wide range of nosocomial pathogenic bacteria.
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : The Department of Biotechnology, India
ID : BT/PR2071/BBE/117/241/2016
Organisme : Indian Council of Medical Research
ID : ICMR-NET-61754/2010
Organisme : RUSA 2.0 Biological Sciences
ID : 311/RUSA (2.0)/2018
Organisme : Bharathidasan University, Tiruchirappalli and Tamil Nadu State Council for Higher Education (TANSCHE)
ID : 01706/P6/2021
Informations de copyright
© 2024 International Union of Biochemistry and Molecular Biology, Inc.
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